TOP2_TRYBB
ID TOP2_TRYBB Reviewed; 1221 AA.
AC P12531;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN Name=TOP2;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2157153; DOI=10.1016/0166-6851(90)90214-7;
RA Strauss P.R., Wang J.C.;
RT "The TOP2 gene of Trypanosoma brucei: a single-copy gene that shares
RT extensive homology with other TOP2 genes encoding eukaryotic DNA
RT topoisomerase II.";
RL Mol. Biochem. Parasitol. 38:141-150(1990).
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; M26803; AAA30256.1; -; Genomic_DNA.
DR PIR; A44978; A44978.
DR AlphaFoldDB; P12531; -.
DR SMR; P12531; -.
DR GO; GO:0020023; C:kinetoplast; IDA:GeneDB.
DR GO; GO:0005634; C:nucleus; ISA:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; ISM:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; ISM:GeneDB.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Topoisomerase.
FT CHAIN 1..1221
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145378"
FT DOMAIN 432..546
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 952..961
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1158..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 771
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 122..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 352..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 466
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 469
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 636
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 637
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 689
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 729
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 770
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 822
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1221 AA; 137594 MW; A88E3E7E153771C2 CRC64;
MAEAHKYKKL TPIEHVLTRP EMYIGSLDTT ATPMFIYDEQ KGHMVWETVK LNHGLLKIVD
EILLNASDNI SNRSARMTYI RVTITDTGEI TIENDGAGIP IVRSREHKLY IPEMVFGHLL
TSSNYDDDNQ NAVAGRHGYG AKLTNILSLS FSVCCRTNGR EFHMSWQDHM RKATAPRVSN
VGTKEKNVTR VKFLPDYERF GMKEKKISND MKRVLYKRIM DLSAMFPNIQ ITLNGSSFGF
KSFKDYATLY SAMTPKGEKP PPPYVYESKS GCVAFIPSVV PGVRRMFGVV NGVVTYNGGT
HCNAAQDILT GCLDGVEREL KKENKVMDTN RVLRHFTILV FLVQVQPKFD SQNKARLVST
PTMPRVPRQD VMKYLLRMPF LEAHVSTITG QLAQELNKEI GTGRRMSSKT LLTSITKLVD
ATSTRRDPKH TRTLIVTEGD SAKALAQNSL SSDQKRYTGV FPLRGKLLNV RNKNLKRLRN
CKELQELFCA LGLELDKDYT DADELRYQRI LIMTDQDADG SHIKGLVINA FESLWPSLLV
RNPGFISIFS TPIVKARLRD KSVVSFFSMK EFHKWQRSNA NTPYTCKYYK GLGTSTTAEG
KEYFKDMEKH TMRLLVDRSD HKLLDNVFDS QEVEWRKDWM TKANAFTGEV DIDRSKKMLT
VTDFVHKEMV HFALVGNARA LAHSVDGLKP SQRKIIWALM RRSGNEAAKV AQLSGYISEA
SAFHHGETSL QETMIKMAQS FTGGNNVNLL VPEGQFGSRQ QLGNDHAAPR YIFTKLSKVA
RLLFPSEDDP LLDYIVEEGQ QVEPNHYVPI LPLLLCNGSV GIGFGFSSNI PPFHRLDVSA
AVRAMISGER AKSVVRRLVP WAVGFQGEIR RGPEGEFIAV GTYTYCKGGR VHVTELPWTC
SVEAFREHIS YLATKDIVNR IADYSGANHV DIDVEVAQGA VNTYAECESE LGLTQRIHIN
GTVFSPNGTL SPLESDLTPV LQWHYDRRLD LYKKRRQRNL TLLEQELARE KSTLKFVQHF
GAGHIDFANA TEATLEKVCS KLGLVRVDDS FDYILRKPIT FYTKTSFENL LKKIAETERR
IEALKKTTPV QLWLGELDQF DRFFQDHEKK MVEAILKERR QRSPPSDLLP GLQQPRLEVE
EAKGGKKFEM RVQVRKYVPP PTKRGAGGRS DGDGGATAAG AAAAVGGRGE KKGPGRAGGV
RRMVLDALAK RVTRLLPRLL F
